SKY_DROME
ID SKY_DROME Reviewed; 587 AA.
AC Q9VIH7; D3DML7; Q8INU4; Q8MSY5; Q8MT51; Q8T0D2;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=GTPase-activating protein skywalker {ECO:0000303|PubMed:21458671};
GN Name=sky {ECO:0000303|PubMed:21458671, ECO:0000312|FlyBase:FBgn0032901};
GN ORFNames=CG9339 {ECO:0000312|FlyBase:FBgn0032901};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL39543.1, ECO:0000312|EMBL:AAM48408.1, ECO:0000312|EMBL:AAM49859.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND F).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ADB91431.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM J).
RA Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-543.
RX PubMed=21458671; DOI=10.1016/j.cell.2011.02.039;
RA Uytterhoeven V., Kuenen S., Kasprowicz J., Miskiewicz K., Verstreken P.;
RT "Loss of skywalker reveals synaptic endosomes as sorting stations for
RT synaptic vesicle proteins.";
RL Cell 145:117-132(2011).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=25422373; DOI=10.1083/jcb.201406026;
RA Fernandes A.C., Uytterhoeven V., Kuenen S., Wang Y.C., Slabbaert J.R.,
RA Swerts J., Kasprowicz J., Aerts S., Verstreken P.;
RT "Reduced synaptic vesicle protein degradation at lysosomes curbs
RT TBC1D24/sky-induced neurodegeneration.";
RL J. Cell Biol. 207:453-462(2014).
RN [7] {ECO:0007744|PDB:5HJN, ECO:0007744|PDB:5HJQ}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-353 IN COMPLEX WITH
RP 1D-MYO-INOSITOL 1,4,5-TRISPHOSPHATE AND SULFATE, FUNCTION, SUBCELLULAR
RP LOCATION, DOMAIN, LIPID BINDING, AND MUTAGENESIS OF ARG-79; ARG-281 AND
RP ARG-335.
RX PubMed=27669036; DOI=10.1038/nsmb.3297;
RA Fischer B., Luthy K., Paesmans J., De Koninck C., Maes I., Swerts J.,
RA Kuenen S., Uytterhoeven V., Verstreken P., Versees W.;
RT "Skywalker-TBC1D24 has a lipid-binding pocket mutated in epilepsy and
RT required for synaptic function.";
RL Nat. Struct. Mol. Biol. 23:965-973(2016).
CC -!- FUNCTION: GTPase-activating protein (GAP) for Rab35 which regulates
CC synaptic vesicle (SV) protein recycling and turnover at the
CC neuromuscular junction boutons and possibly ventral nerve cord via
CC endosomal trafficking (PubMed:21458671, PubMed:25422373,
CC PubMed:27669036). Inhibits Rab35-mediated endosomal sorting which
CC traffics old or dysfunctional SV proteins through a degradative
CC endolysosomal route that involves the ESCRT pathway and the HOPS
CC complex members dor, vps39 and rab7 (PubMed:21458671, PubMed:25422373).
CC This function is essential for preventing excessive degradation and
CC turnover of vesicles from the readily releasable pool which leads to
CC increased neurotransmission and eventually neurodegeneration
CC (PubMed:21458671, PubMed:25422373, PubMed:27669036). Preferentially
CC binds phosphoinositides phosphorylated at the D5 position of the
CC inositol ring, such as phosphatidylinositol 4,5-bisphosphate (PIP2) and
CC phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed:27669036).
CC Binding to phosphoinositides and thus membrane-association, is required
CC for its function in regulating the turnover of synaptic-vesicle
CC proteins (PubMed:27669036). It is therefore likely that it is recruited
CC to vesicle membranes with high phosphoinositide content and thereby
CC selectively prevents endolysosomal degradation of these vesicles
CC (PubMed:27669036). {ECO:0000269|PubMed:21458671,
CC ECO:0000269|PubMed:25422373, ECO:0000269|PubMed:27669036}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:21458671,
CC ECO:0000269|PubMed:27669036}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21458671, ECO:0000269|PubMed:27669036}. Endosome
CC membrane {ECO:0000269|PubMed:21458671}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21458671}. Note=Detected at the synapses of
CC neuromuscular junction boutons, where it displays co-localization with
CC Rab35 (PubMed:21458671). Associates with certain types of membrane
CC phosphoinositides such as phosphatidylinositol 4,5-bisphosphate (PIP2)
CC and phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed:27669036).
CC {ECO:0000269|PubMed:21458671, ECO:0000269|PubMed:27669036}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A {ECO:0000312|FlyBase:FBgn0032901};
CC IsoId=Q9VIH7-1; Sequence=Displayed;
CC Name=J {ECO:0000312|FlyBase:FBgn0032901};
CC IsoId=Q9VIH7-2; Sequence=VSP_059919;
CC Name=F {ECO:0000312|FlyBase:FBgn0032901}; Synonyms=I
CC {ECO:0000312|FlyBase:FBgn0032901};
CC IsoId=Q9VIH7-3; Sequence=VSP_059917, VSP_059918;
CC -!- TISSUE SPECIFICITY: Detected in the larval ventral nerve cord and
CC neuromuscular junction boutons (at protein level).
CC {ECO:0000269|PubMed:21458671}.
CC -!- DOMAIN: The Rab-GAP TBC domain is essential for phosphoinositide
CC binding. {ECO:0000269|PubMed:27669036}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM49859.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53942.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF53945.2; -; Genomic_DNA.
DR EMBL; AE014134; AAS64731.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11097.2; -; Genomic_DNA.
DR EMBL; AE014134; ACZ94312.1; -; Genomic_DNA.
DR EMBL; AE014134; AGB93184.1; -; Genomic_DNA.
DR EMBL; AY069398; AAL39543.1; -; mRNA.
DR EMBL; AY118379; AAM48408.1; -; mRNA.
DR EMBL; AY118490; AAM49859.1; ALT_INIT; mRNA.
DR EMBL; BT120183; ADB91431.1; -; mRNA.
DR RefSeq; NP_001163026.1; NM_001169555.1. [Q9VIH7-3]
DR RefSeq; NP_001260649.1; NM_001273720.1. [Q9VIH7-2]
DR RefSeq; NP_610073.1; NM_136229.5. [Q9VIH7-1]
DR RefSeq; NP_724302.1; NM_165350.4. [Q9VIH7-1]
DR RefSeq; NP_724303.2; NM_165351.4. [Q9VIH7-3]
DR RefSeq; NP_995738.1; NM_206016.3. [Q9VIH7-1]
DR PDB; 5HJN; X-ray; 2.50 A; A=1-353.
DR PDB; 5HJQ; X-ray; 2.30 A; A=1-353.
DR PDB; 6R82; X-ray; 2.05 A; A/B=401-587.
DR PDBsum; 5HJN; -.
DR PDBsum; 5HJQ; -.
DR PDBsum; 6R82; -.
DR AlphaFoldDB; Q9VIH7; -.
DR SMR; Q9VIH7; -.
DR IntAct; Q9VIH7; 1.
DR STRING; 7227.FBpp0303287; -.
DR TCDB; 8.A.126.1.2; the nuclear receptor coactivator 7 (ncoa7) family.
DR DNASU; 35359; -.
DR EnsemblMetazoa; FBtr0081441; FBpp0080970; FBgn0032901. [Q9VIH7-1]
DR EnsemblMetazoa; FBtr0081442; FBpp0080971; FBgn0032901. [Q9VIH7-1]
DR EnsemblMetazoa; FBtr0081445; FBpp0080974; FBgn0032901. [Q9VIH7-3]
DR EnsemblMetazoa; FBtr0081447; FBpp0080976; FBgn0032901. [Q9VIH7-1]
DR EnsemblMetazoa; FBtr0301961; FBpp0291173; FBgn0032901. [Q9VIH7-3]
DR EnsemblMetazoa; FBtr0330255; FBpp0303287; FBgn0032901. [Q9VIH7-2]
DR GeneID; 35359; -.
DR KEGG; dme:Dmel_CG9339; -.
DR UCSC; CG9339-RA; d. melanogaster. [Q9VIH7-1]
DR UCSC; CG9339-RE; d. melanogaster.
DR CTD; 35359; -.
DR FlyBase; FBgn0032901; sky.
DR VEuPathDB; VectorBase:FBgn0032901; -.
DR eggNOG; KOG2801; Eukaryota.
DR GeneTree; ENSGT00410000025739; -.
DR HOGENOM; CLU_018035_1_1_1; -.
DR Reactome; R-DME-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 35359; 0 hits in 1 CRISPR screen.
DR ChiTaRS; sky; fly.
DR GenomeRNAi; 35359; -.
DR PRO; PR:Q9VIH7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032901; Expressed in brain and 11 other tissues.
DR ExpressionAtlas; Q9VIH7; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IMP:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IMP:UniProtKB.
DR GO; GO:1903422; P:negative regulation of synaptic vesicle recycling; IMP:UniProtKB.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0031175; P:neuron projection development; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:FlyBase.
DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP:UniProtKB.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR006571; TLDc_dom.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF07534; TLD; 1.
DR SMART; SM00164; TBC; 1.
DR SMART; SM00584; TLDc; 1.
DR SUPFAM; SSF47923; SSF47923; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
DR PROSITE; PS51886; TLDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle; Endosome;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..587
FT /note="GTPase-activating protein skywalker"
FT /id="PRO_0000445623"
FT DOMAIN 84..275
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 408..585
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT BINDING 75
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000269|PubMed:27669036,
FT ECO:0007744|PDB:5HJQ"
FT BINDING 79
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000269|PubMed:27669036,
FT ECO:0007744|PDB:5HJQ"
FT BINDING 277
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000269|PubMed:27669036,
FT ECO:0007744|PDB:5HJQ"
FT BINDING 281
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000269|PubMed:27669036,
FT ECO:0007744|PDB:5HJQ"
FT BINDING 335..339
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000269|PubMed:27669036,
FT ECO:0007744|PDB:5HJQ"
FT VAR_SEQ 1..50
FT /note="MPYHRGGDASSQADKLSGIVEESDLYEGFAPHVETSEIKTLDFYNLPKQT
FT -> MVGKVLGIKDLEQFSSRRSSVYVDPECDKFFELPLFIAASSNDITTKCQCFQFSP
FT (in isoform F)"
FT /id="VSP_059917"
FT VAR_SEQ 396..414
FT /note="Missing (in isoform F)"
FT /id="VSP_059918"
FT VAR_SEQ 396..414
FT /note="HFGLPGTKNFIKTWTDRQF -> KLHSESCRNLGEKSPGHRAIAMGVYPIHN
FT LKSQACKNED (in isoform J)"
FT /id="VSP_059919"
FT MUTAGEN 79
FT /note="R->C: Loss of binding to liposomes containing
FT phosphoinositides. In contrast to wild-type protein whose
FT expression largely rescues mutant phenotypes, expression in
FT mutant neurons only partially rescues the increase in
FT synapse mobility and the abherent accumulation of large
FT cisternal or endosomal-like structures in pre-synaptic
FT terminals observed in mutants. In addition, the number of
FT mutants displaying defective motor coordination, defective
FT flight, hyperactivity, increased temperature sensitivity
FT and seziures is increased compared to mutants expressing
FT wild-type protein."
FT /evidence="ECO:0000269|PubMed:27669036"
FT MUTAGEN 281
FT /note="R->C: Reduced binding to liposomes under low
FT phosphatidylinositol 4,5-bisphosphate (PIP2)
FT concentrations. Reduced binding to inositol 1,4,5-
FT trisphosphate (IP3). In contrast to wild-type, expression
FT only partially rescues the accumulation of sub-boutonic
FT foci."
FT /evidence="ECO:0000269|PubMed:27669036"
FT MUTAGEN 335
FT /note="R->P: Little effect on binding to liposomes,
FT phosphatidylinositol 4,5-bisphosphate and inositol 1,4,5-
FT trisphosphate."
FT /evidence="ECO:0000269|PubMed:27669036"
FT MUTAGEN 543
FT /note="G->R: In sky-1; embryonic lethal."
FT /evidence="ECO:0000269|PubMed:21458671"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:5HJQ"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5HJN"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5HJN"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:5HJQ"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:5HJQ"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:5HJQ"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 277..294
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5HJN"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:5HJQ"
FT TURN 339..343
FT /evidence="ECO:0007829|PDB:5HJQ"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:6R82"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:6R82"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:6R82"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 429..436
FT /evidence="ECO:0007829|PDB:6R82"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:6R82"
FT HELIX 444..451
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:6R82"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 499..506
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:6R82"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 545..549
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:6R82"
FT TURN 561..564
FT /evidence="ECO:0007829|PDB:6R82"
FT STRAND 568..585
FT /evidence="ECO:0007829|PDB:6R82"
SQ SEQUENCE 587 AA; 67328 MW; 54E1543FCA208164 CRC64;
MPYHRGGDAS SQADKLSGIV EESDLYEGFA PHVETSEIKT LDFYNLPKQT GKEPALRSYT
EIQQLLQQGK KRDVKNILRE NSWPINSPIR AQLWPMLCGQ HQTKQQMLDG FYWEMVHQVF
GTTELSEKPI MLPAFVDATH CLPYHLTSTG RAVADRIVNV LGYDCPDITY SPVLYPITSI
LLHFMSEEEA YICLAGLVGS KEKVFINQTK LQHEVTWKTV MQIAKKHTKS ATSYFQRICP
GLKLERIFMD WCWWILAGLP FQHLVRIMDC YFHEGIKVLY RVALVILNLF HKECQSNNEW
SPDNIKNDIG NALIKFCKKI PVSPAKLLHA AFSIRGLSTQ YISRIFIKTE MLLKSRSVLT
SGSKQLIKSR SSDNLPTSQS QVNIQMMSHT LTIREHFGLP GTKNFIKTWT DRQFLFTLWS
WLPVRITMYQ PVLLYTTEEH GCSLTTFYVR VEQHEPTLLM IKTCNNEVFG AYCSSRWFER
NVKDDKGQRQ AYFGTGETFL FSLYPERAKY PWVGIEGDKD LGHSSELFMA ADSKMITIGG
GEGQAIWMDE NIRFGKTDSC KTFNNPPLCP SGDFEIRVLE VYGFVGI
